Hop: More than an Hsp70/Hsp90 adaptor protein

BioEssays

Volumn 26, Issue 10, 2004, Pages 1058-1068

  Odunuga, O O ^a   Longshaw, V M ^b   Blatch, G L ^b  

^a UNIVERSITY OF CAPE TOWN   (South Africa)

^b RHODES UNIVERSITY   (South Africa)

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; CHAPERONE; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; HSP70 HSP90 ORGANIZING PROTEIN; PRION PROTEIN; UNCLASSIFIED DRUG;

CELL DIVISION; CELL FUNCTION; CRYSTAL STRUCTURE; ENZYME ACTIVITY; GENE ACTIVITY; GENETIC TRANSCRIPTION; HUMAN; NONHUMAN; NUCLEOCYTOPLASMIC TRANSPORT; NUCLEOTIDE SEQUENCE; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN TRANSPORT; REVIEW; SEQUENCE HOMOLOGY; SIGNAL TRANSDUCTION; STRESS; STRUCTURE ANALYSIS; VIRUS REPLICATION;

AMINO ACID SEQUENCE; ANIMALS; HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; HSP90 HEAT-SHOCK PROTEINS; HUMANS; MODELS, MOLECULAR; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; SUBCELLULAR FRACTIONS;

HUMULUS;

EID: 7044240678     PISSN: 02659247     EISSN: None     Source Type: Journal    
DOI: 10.1002/bies.20107     Document Type: Review

References (81)

1. Nicolet CM, Craig EA. 1989. Isolation and characterization of STI1, a stress-inducible gene from Saccharomyces cerevisiae. Mol Cell Biol 9:3638-3646.
2. Honore B, Leffers H, Madsen P, Rasmussen HH, Vandeckerckhove J, et al. 1992. Molecular cloning and expression of a transformation-sensitive human protein containing TPR motif and sharing identity to the stress-inducible yeast protein STI1. J Biol Chem 267:8485-8491.
3. Blatch GL, Lässte M, Zetter BR, Kundra V. 1997. Isolation of a mouse cDNA encoding mSTI1, a stress-inducible protein containing the TPR motif. Gene 194:277-282.
4. Demand J, Luders J, Hohfeld J. 1998. The carboxy-terminal domain of Hsc70 provides binding sites for a distinct set of chaperone cofactors. Mol Cell Biol 18:2023-2028.
5. Adams MD, Celniker SE, Holt RA, Evans CA, Gocayne JD, et al. 2000. The genome sequence of Drosophila melanogaster. Science 287:2185-2195.
6. Wood V, Gwilliam R, Rajandream MA, Lyne M, Lyne R, et al. 2002. The genome sequence of Schizosaccharomyces pombe. Nature 415:871-880.
7. Zhang Z, Quick MK, Kanelakis KC, Gijzen M, Krishna P. 2003. Characterization of a plant homolog of hop, a cochaperone of hsp90. Plant Physiol 131:525-535.
8. Hernandez Torres J, Chatellard P, Stutz E. 1995. Isolation and characterization of gmsti, a stress-inducible gene from soybean (Glycine max) coding for a protein belonging to the TPR (tetratricopeptide repeats) family. Plant Mol Biol 27:1221-1226.
9. Carlton JM, Angiuoli SV, Suh BB, Kooij TW, Pertea M, et al. 2002. Genome sequence and comparative analysis of the model rodent malaria parasite Plasmodium yoelii yoelii. Nature 419:512-519.
10. Joshi M, Dwyer DM, Nakhasi HL. 1993. Cloning and characterization of differentially expressed genes in vitro-grown 'amastigotes' of Leishmania donovani. Mol Biochem Parasitol 58:345-354.
11. Webb JR, Campos-Neto A, Skeiky YAW, Reed SG. 1997. Molecular characterization of the heat-inducible LmSTI1 protein of Leishmania major. Mol Biochem Parasitol 89:179-193.
12. Cheng CH, Liu SM, Chow TY, Hsiao YY, Wang DP, et al. 2002. Analysis of the complete genome sequence of the Hz-1 virus suggests that it is related to members of the Baculoviridae. J Virol 76:9024-9034.
13. Smith DF, Sullivan WP, Marion TN, Zaitsu K, Madden B, et al. 1993. Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70. Mol Cell Biol 13:869-876.
14. Krishna P, Gloor G. 2001. The Hsp90 family of proteins in Arabidopsis thaliana. Cell Stress Chaperones 6:238-246.
15. Blatch GL, Lässle M. 1999. The tetratricopeptide repeat, a structural motif mediating protein-protein interactions. BioEssays 21:932-939.
16. Chang H-CJ, Nathan DF, Lindquist S. 1997. In vivo analysis of the Hsp90 cochaperone Stil (p60). Mol Cell Biol 17:318-325.
17. Chen S, Prapapanich V, Rimerman RA, Honoré B, Smith DF. 1996. Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins Hsp90 and Hsp70. Mol Endocrinol 10:682-693.
18. Chen S, Smith DF. 1998. Hsp90 and adaptor in the heat shock protein 70 (Hsp70) and Hsp90 chaperone machinery. J Biol Chem 273:35194-35200.
19. Bose S, Weikl T, Bugl H, Buchner J. 1996. Chaperone function of Hsp90-associated proteins. Science 274:1715-1717.
20. Dittmar KD, Hutchison KA, Owens-Grillo JK, Pratt WB. 1996. Reconstitution of the steroid receptor.hsp90 heterocomplex assembly system of rabbit reticulocyte lysate. J Biol Chem 271:12833-12839.
21. Rajapandi T, Greene LE, Eisenberg E. 2000. The molecular chaperones Hsp90 and Hsc70 are both necessary and sufficient to activate hormone binding by glucocorticoid receptor. J Biol Chem 275:22597-22604.
22. Morishima Y, Kanelakis KC, Silverstein AM, Dittmar KD, Estrada L, et al. 2000. The Hsp organizer protein Hop enhances the rate of but is not essential for glucocorticoid receptor folding by the multiprotein Hsp90-based chaperone system. J Biol Chem 275:6894-6900.
23. Gross M, Hessefort S. 1996. Purification and characterization of a 66-kDa protein from rabbit reticulocyte lysate which promotes the recycling of Hsp. J Biol Chem 271:16833-16841.
24. Wegele H, Haslbeck M, Reinstein J, Buchner J. 2003. Sti1 is a novel activator of the Ssa proteins. J Biol Chem 278:25970-25976.
25. Owens-Grillo JK, Czar MJ, Hutchison KA, Hoffman K, Perdew GH, et al. 1996. A model of protein targeting mediated by immunophilins and other proteins that bind to hsp90 via tetratricopeptide repeat domains. J Biol Chem 271:13468-13475.
26. Abbas-Terki T, Briand P-A, Donzé O, Picard D. 2002. The Hsp90 co-chaperones Cdc37 and Stil interact physically and genetically. Biol Chem 383:1335-1342.
27. Glover JR, Lindquist S. 1998. Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94:73-82.
28. Abbas-Terki T, Donzé O, Briand P-A, Picard D. 2001. Hsp104 interacts with Hsp90 cochaperones in respiring yeast. Mol Cell Biol 21:7569-7575.
29. Martins VR, Graner E, Garcia-Abreu J, de Souza SJ, Mercadante AF, et al. 1997. Complementary hydropathy identifies a cellular prion protein receptor. Nat Med 3:1376-1382.
30. Zanata SM, Lopes MH, Mercadante AF, Hajj GN, Chiarini LB, et al. 2002. Stress-inducible protein 1 is a cell surface ligand for cellular prion that triggers neuroprotection. EMBO J 21:3307-3316.
31. Lässle M, Blatch GL, Kundra V, Takatori T, Zetter BR. 1997. Stress-inducible, murine protein mSTI1: Characterization of binding domains for heat shock proteins and in vitro phosphorylation by different kinases. J Biol Chem 272:1876-1884.
32. Longshaw VM, Dirr HW, Blatch GL, Lässle M. 2000. The in vitro phosphorylation of the co-chaperone mSTI1 by cell cycle kinases substantiates a predicted casein kinase II-p34cdc2-NLS (CcN) motif. Biol Chem 381:1133-1138.
33. Longshaw VM, Chapple JP, Balda MS, Cheetham ME, Blatch GL. 2004. The nuclear translocation of the Hsp70/Hsp90 organizing protein mSTI1 is regulated by cell cycle kinases. J Cell Sci 117:701-710.
34. Zheng L, Roeder RG, Luo Y. 2003. S phase activation of the histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component. Cell 114:255-266.
35. Freeman BC, Toft DO, Morimoto RI. 1996. Molecular chaperone machines: chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23. Science 274:1718-1720.
36. Dolinski KJ, Cardenas ME, Heitman J. 1998. CNSI encodes an essential p60/sti1 homolog in Saccharomyces cerevisiae that suppresses cyclophilin 40 mutations and interacts with hsp90. Mol Cell Biol 18:7344-7352.
37. Duina AA, Chang H-CJ, Marsh JA, Lindquist S, Gaber RF. 1996. A cyclophilin function in Hsp90-dependent signal transduction. Science 274:1713-1715.
38. Fang Y, Fliss AE, Rao J, Caplan AJ. 1998. SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23. Mol Cell Biol 18:3727-3734.
39. Jones MH, Bachant JB, Castillo AR, Giddings THJ, Winey M. 1999. Yeast Damp1 is required to maintain spindle integrity during mitosis and interacts with the Mps1 kinase. Mol Biol Cell 10:2377-2391.
40. Liu XD, Morano KA, Thiele DJ. 1999. The yeast Hsp110 family member, Ssel, is an Hsp90 cochaperone. J Biol Chem 274:26654-26660.
41. Stancato LF, Hutchison KA, Krishna P, Pratt WB. 1996. Animal and plant cell lysates share a conserved chaperone system that assembles the glucocorticoid receptor into a functional heterocomplex with hsp90. Biochemistry 35:554-561.
42. Cheung J, Smith DF. 2000. Molecular chaperone interactions with steroid receptors: an update. Mol Endocrinol 14:939-946.
43. Hernández MP, Sullivan WP, Toft DO. 2002. The assembly and intermolecular properties of the hsp70-Hop-hsp90 molecular chaperone complex. J Biol Chem 277:38294-38304.
44. Johnson BD, Schumacher RJ, Ross ED, Toft DO. 1998. Hop modulates hsp70/hsp90 interactions in protein folding. J Biol Chem 273:3679-3686.
45. Gebauer M, Melki R, Gehring U. 1998. The chaperone cofactor Hop/p60 interacts with the cytosolic chaperonin-containing TCP-1 and affects its nucleotide exchange and protein folding activities. J Biol Chem 273:29475-29480.
46. Brinker A, Scheufler C, von der Mülbe F, Fleckenstein B, Herrmann C, et al. 2002. Ligand discrimination by TPR domains: relevance and selectivity of EEVD-recognition in Hsp70 Hop Hsp90 complexes. J Biol Chem 277:19265-19275.
47. Odunuga OO, Hornby JA, Bies C, Zimmermann R, Pugh DJ, et al. 2003. Tetratricopeptide repeat motif-mediated Hsc70-mSTI1 interaction: molecular characterization of the critical contacts for successful binding and specificity. J Biol Chem 278:6896-6904.
48. Young JC, Moarefi I, Hartl FU. 2001. Hsp90: a specialized but essential protein-folding tool. J Cell Biol 154:267-273.
49. Murphy PJM, Kanelakis KC, Galigniana MD, Morishima Y, Pratt WB. 2001. Stoichiometry, abundance, and functional significance of the hsp90/hsp70-based multiprotein chaperone machinery in reticulocyte lysate. J Biol Chem 276:30092-30098.
50. Silverstein AM, Galigniana MD, Kanelakis KC, Radanyi C, Renoir JM, Pratt WB. 1999. Different regions of the immunophilin FKBP52 determine its association with the glucocorticoid receptor, hsp90, and cytoplasmic dynein. J Biol Chem 274:36980-36986.
51. Rutherford SL, Lindquist S. 1998. Hsp90 as a capacitor for morphological evolution. Nature 396:336-342.
52. Sangster TA, Lindquist S, Queitsch C. 2004. Under cover: causes, effects and implications of Hsp90-mediated genetic capacitance. BioEssays 26:348-362.
53. Prodromou C, Siligardi G, O'Brien R, Woolfson DN, Regan L, et al. 1999. Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones. EMBO J 18:754-762.
54. Richter K, Muschler P, Hainzl O, Reinstein J, Buchner J. 2003. Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the ATPase cycle. J Biol Chem 278:10328-10333.
55. cdc37. J Biol Chem 277:20151-20159.
56. McLaughlin SH, Smith HW, Jackson SE. 2002. Stimulation of the weak ATPase activity of human Hsp90 by a client protein. J Mol Biol 315:787-798.
57. Kamal A, Thao L, Sensintaffar J, Zhang L, Boehm MF, et al. 2003. A high-affinity conformation of Hsp90 confers tumor selectivity on Hsp90 inhibitors. Nature 425:357-359.
58. Piper PW, Panaretou B, Millson SH, Trumana A, Mollapour M, et al. 2003. Yeast is selectively hypersensitised to heat shock protein 90 (Hsp90)-targetting drugs with heterologous expression of the human Hsp90beta, a property that can be exploited in screens for new Hsp90 chaperone inhibitors. Gene 302:165-170.
59. Sikorski RS, Boguski MS, Goebl M, Hieter P. 1990. A repeating amino acid motif in CDC23 defines a family of proteins and a new relationship among genes required for mitosis and RNA synthesis. Cell 60:307-317.
60. Goebl M, Yanagida M. 1991. The TPR snap helix: a novel protein repeat motif from mitosis to transcription. Trends Biochem Sci 16:173-177.
61. Das AK, Cohen PTW, Barford D. 1998. The structure of the tetratricopeptide repeats of protein phosphatase 5, implications for TPR-mediated protein-protein interactions. EMBO J 17:1192-1199.
62. Scheufler C, Brinker A, Bourenkov G, Pegoraro S, Moroder L, et al. 2000. Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell 101:199-210.
63. van der Spuy J, Kana BD, Dirr HW, Blatch GL. 2000. Heat shock cognate protein 70 chaperone-binding site in the co-chaperone murine stress-inducible protein 1 maps to within three consecutive tetratricopeptide repeat motifs. Biochem J 345:645-651.
64. phox in complex with Rac.GTP. Mol Cell 6:899-907.
65. Gounalaki N, Tzamarias D, Vlassi M. 2000. Identification of residues in the TPR domain of Ssn6 responsible for interaction with the Tup1 protein. FEBS Lett 473:37-41.
66. Carrigan PE, Nelson GM, Roberts PJ, Stoffer J, Riggs DL, et al. 2004. Multiple domains of the co-chaperone Hop are important for Hsp70 binding. J Biol Chem 279:16185-16193.
67. Liu F-H, Wu S-J, Hu S-M, Hsiao C-D, Wang C. 1999. Specific interaction of the 70-kDa heat shock cognate protein with the tetratricopeptide repeats. J Biol Chem 274:34425-34432.
68. Nelson GM, Huffman H, Smith DF. 2003. Comparison of the carboxyterminal DP-repeat region in the co-chaperones Hop and Hip. Cell Stress Chap 8:125-133.
69. Gross M, Hessefort S, Olin A, Reddy G. 1996. Extensive sequencing of tryptic peptides of a rabbit reticulocyte 66-kDa protein that promotes recycling of Hsp70. J Biol Chem 271:16842-16849.
70. Cheung-Flynn J, Roberts PJ, Riggs DL, Smith DF. 2003. C-terminal sequences outside the tetratricopeptide repeat domain of FKBP51 and FKBP52 cause differential binding to Hsp90. J Biol Chem 278:17388-17394.
71. Hu J, Toft D, Anselmo D, Wang X. 2002. In vitro reconstitution of functional hepadnavirus reverse transcriptase with cellular chaperone proteins. J Virol 76:269-279.
72. Arbeitman MN, Hogness DS. 2000. Molecular chaperones activate the Drosophila ecdysone receptor, and RXR heterodimer. Cell 101:67-77.
73. Kryndushkin D, Smirnov VN, Ter-Avanesyan MD. 2002. Increased expression of Hsp40 chaperones, transcriptional factors, and ribosomal protein Rpp0 can cure yeast prions. J Biol Chem 277:23702-23708.
74. Song J, Takeda M, Morimoto RI. 2001. Bag1-Hsp70 mediates a physiological stress signalling pathway that regulates Raf-1/ERK and cell growth. Nat Cell Biol 3:276-82.
75. Nollen EAA, Morimoto RI. 2002. Chaperoning signalling pathways: molecular chaperones as stress-sensing 'heat shock' proteins. J Cell Sci 115:2809-2816.
76. Bharadwaj S, Ali A, Ovsenek N. 1999. Multiple components of the HSP90 chaperone complex function in regulation of heat shock factor 1 in vivo. Mol Cell Biol 19:8033-8041.
77. Donzé O, Picard D. 1999. Hsp90 binds and regulates the ligand-inducible a subunit of eukatyotic translation initiation factor kinase Gcn2. Mol Cell Biol 19:8422-8432.
78. Scholz GM, Cartledge K, Hall NE. 2001. Identification and characterization of Harc: a novel Hsp90 associating relative of Cdc37. J Biol Chem 276:30971-30979.
79. Yamashita YM, Nakaseko Y, Samejima I, Kumada K, Yamada H, et al. 1996. 20S cyclosome complex formation and proteolytic activity inhibited by the cAMP/PKA pathway. Nature 384:276-279.
80. Thompson JD, Higgins DG, Gibson TJ. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nuc Acid Res 22:4673-4680.
81. Kraulis PJ. 1991. MOLSCRIPT, a program to produce both detailed and schematic plots of protein structures. J App Cryst 24:946-950.